Structure of PDB 4v8r Chain AB

Receptor sequence
>4v8rAB (length=517) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
QIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSNT
CMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAELL
REAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDL
IHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKL
SDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVD
STAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGI
NSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQPF
LKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVLG
GGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDSS
ELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSASE
AAEVLLRVDNIIRARPR
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAB
Resolution3.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP AB L37 P39 D90 G91 T93 S94 T159 G404 L444 I487 E489 K494 L34 P36 D87 G88 T90 S91 T156 G401 L441 I484 E486 K491
BS02 BEF AB D90 T92 T93 K164 D87 T89 T90 K161
BS03 MG AB D90 T160 D87 T157
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP39076|TCPB_YEAST T-complex protein 1 subunit beta (Gene Name=CCT2)

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